The myelin sheath is a multilayered membrane wrapped around axons in the vertebrate nervous system; it enables the rapid transmission of nerve impulses. It contains a set of specific proteins, which are involved in myelin formation and linked to neurological diseases. Two such proteins are studied here: P2 and CNPase. We aim to study the dynamics of these proteins, with the aim of linking the results to our wealth of other structure-function data on these molecules. For P2, our interest lies in the effects of a functionally relevant hinge-region mutation P38G on the protein dynamics. For CNPase, we are interested in the effects of active site mutations and ligands on protein dynamics. The proposed experiments are a part of a PhD project funded by the European Spallation Source (ESS).